Research ArticleHIV

Antigen-specific antibody Fc glycosylation enhances humoral immunity via the recruitment of complement

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Science Immunology  17 Aug 2018:
Vol. 3, Issue 26, eaat7796
DOI: 10.1126/sciimmunol.aat7796

Sweetening up antibodies

Certain individuals (neutralizers) infected with HIV are able to generate broadly neutralizing antibodies more efficiently than others (non-neutralizers). By comparing HIV-specific antibodies isolated from neutralizers and non-neutralizers, Lofano et al. found sialylation of the Fc domain to be higher in neutralizers. To understand the biological functions of Fc domain sialylation, the authors generated sialylated and nonsialylated isoforms of an HIV gp120-specific antibody, PGT121. By generating immune complexes of sialylated or nonsialylated PGT121 bound to fluorescently labeled HIV gp120, they found that sialylation enhanced the deposition of antigen in B cell follicles in a complement-dependent manner. Besides stressing the importance of the Fc domain in regulating antibody functions, the study also highlights the role of the complement pathway in driving humoral immunity.

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